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P81065

- GST_OCHAN

UniProt

P81065 - GST_OCHAN

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Protein

Glutathione S-transferase

Gene

gst

Organism
Ochrobactrum anthropi
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Kineticsi

  1. KM=0.132 mM for glutathione1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glutathione1 Publication
Binding sitei35 – 351Glutathione1 Publication
Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei105 – 1051Glutathione1 Publication

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase (EC:2.5.1.18)
Gene namesi
Name:gst
OrganismiOchrobactrum anthropi
Taxonomic identifieri529 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101C → A: Strongly reduced affinity for glutathione. Reduces enzyme activity by about 50%. 1 Publication
Mutagenesisi11 – 111S → A: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Glutathione S-transferasePRO_0000185973Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi12 – 2110Combined sources
Beta strandi26 – 294Combined sources
Turni32 – 354Combined sources
Helixi43 – 453Combined sources
Beta strandi54 – 585Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 7510Combined sources
Helixi80 – 823Combined sources
Helixi89 – 10921Combined sources
Helixi110 – 1123Combined sources
Helixi118 – 13821Combined sources
Beta strandi148 – 1503Combined sources
Helixi153 – 16715Combined sources
Helixi176 – 18611Combined sources
Helixi189 – 1979Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NTOX-ray2.10A1-201[»]
2PVQX-ray1.80A1-201[»]
ProteinModelPortaliP81065.
SMRiP81065. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81065.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8181GST N-terminalAdd
BLAST
Domaini87 – 201115GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 662Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Beta family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13409. GST_N_2. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81065-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLYYKVGAC SLAPHIILSE AGLPYELEAV DLKAKKTADG GDYFAVNPRG
60 70 80 90 100
AVPALEVKPG TVITQNAAIL QYIGDHSDVA AFKPAYGSIE RARLQEALGF
110 120 130 140 150
CSDLHAAFSG LFAPNLSEEA RAGVIANINR RLGQLEAMLS DKNAYWLGDD
160 170 180 190 200
FTQPDAYASV IIGWGVGQKL DLSAYPKALK LRERVLARPN VQKAFKEEGL

N
Length:201
Mass (Da):21,739
Last modified:May 30, 2000 - v2
Checksum:i763B2D3DECA21F2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17279 Genomic DNA. Translation: CAA76728.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17279 Genomic DNA. Translation: CAA76728.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NTO X-ray 2.10 A 1-201 [» ]
2PVQ X-ray 1.80 A 1-201 [» ]
ProteinModelPortali P81065.
SMRi P81065. Positions 1-201.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P81065.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF13409. GST_N_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi."
    Favaloro B., Tamburro A., Angelucci S., de Luca A., di Ilio C., Rotilio D.
    Biochem. J. 335:573-579(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25 AND 50-74, MUTAGENESIS.
  2. "Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi."
    Favaloro B., Melino S., Petruzzelli R., di Ilio C., Rotilio D.
    FEMS Microbiol. Lett. 160:81-86(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-25.
  3. "Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site."
    Allocati N., Federici L., Masulli M., Favaloro B., Di Ilio C.
    Proteins 71:16-23(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-10, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiGST_OCHAN
AccessioniPrimary (citable) accession number: P81065
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3